3D local structure around copper site of rabbit prion-related protein: Quantitative determination by XANES spectroscopy combined with multiple-scattering calculations
Cui, P. X.1,2; Lian, F. L.5; Wang, Y.1,2; Wen, Yi5; Chu, W. S.1,2; Zhao, H. F.2; Zhang, S.4; Li, J.4; Lin, D. H.3; Wu, Z. Y.1,2
刊名RADIATION PHYSICS AND CHEMISTRY
2014-02
卷号95页码:69-72
关键词RaPrP Copper XANES MXAN EXAFS
ISSN号0969-806X
DOI10.1016/j.radphyschem.2013.01.043
文献子类Article
英文摘要Prion-related protein (PrP), a cell-surface copper-binding glycoprotein, is considered to be responsible for a number of transmissible spongiform encephalopathies (TSEs). The structural conversion of PrP from the normal cellular isoform (PrPC) to the post-translationally modified form (PrPSc) is thought to be relevant to Cu2+ binding to histidine residues. Rabbits are one of the few mammalian species that appear to be resistant to TSEs, because of the structural characteristics of the rabbit prion protein (RaPrPC) itself. Here we determined the three-dimensional local structure around the C-terminal high-affinity copper-binding sites using X-ray absorption near-edge structure combined with ab initio calculations in the framework of the multiple-scattering (MS) theory. Result shows that two amino acid resides, Gln97 and Met108, and two histidine residues, His95 and His110, are involved in binding this copper(II) ion. It might help us understand the roles of copper in prion conformation conversions, and the molecular mechanisms of prion-involved diseases. (C) 2013 Elsevier Ltd. All rights reserved.
资助项目Knowledge Innovation Program of the Chinese Academy of Sciences[KJCX2-YW-N42] ; Key Important Project of the National Natural Science Foundation of China[10734070] ; National Natural Science Foundation of China[NSFC 10805055] ; National Natural Science Foundation of China[11275227] ; National Natural Science Foundation of China[31170717] ; National Natural Science Foundation of China[91129713] ; National Basic Research Program of China[2009CB930804]
WOS关键词X-RAY-ABSORPTION ; SPECTRA ; SCRAPIE
WOS研究方向Chemistry ; Nuclear Science & Technology ; Physics
语种英语
出版者PERGAMON-ELSEVIER SCIENCE LTD
WOS记录号WOS:000329271400016
内容类型期刊论文
源URL[http://119.78.100.183/handle/2S10ELR8/277215]  
专题分析化学研究室
通讯作者Chu, W. S.
作者单位1.Univ Sci & Technol China, Natl Synchrotron Radiat Lab, Hefei 230029, Peoples R China;
2.Inst High Energy Phys, Beijing Synchrotron Radiat Facil, Beijing 100049, Peoples R China;
3.Xiamen Univ, Key Lab Chem Biol Fujian Prov, Coll Chem & Chem Engn, Xiamen 361005, Peoples R China;
4.Shanghai Inst Appl Phys, Shanghai Synchrotron Radiat Facil, Shanghai 201204, Peoples R China
5.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China;
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Cui, P. X.,Lian, F. L.,Wang, Y.,et al. 3D local structure around copper site of rabbit prion-related protein: Quantitative determination by XANES spectroscopy combined with multiple-scattering calculations[J]. RADIATION PHYSICS AND CHEMISTRY,2014,95:69-72.
APA Cui, P. X..,Lian, F. L..,Wang, Y..,Wen, Yi.,Chu, W. S..,...&Wu, Z. Y..(2014).3D local structure around copper site of rabbit prion-related protein: Quantitative determination by XANES spectroscopy combined with multiple-scattering calculations.RADIATION PHYSICS AND CHEMISTRY,95,69-72.
MLA Cui, P. X.,et al."3D local structure around copper site of rabbit prion-related protein: Quantitative determination by XANES spectroscopy combined with multiple-scattering calculations".RADIATION PHYSICS AND CHEMISTRY 95(2014):69-72.
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